ID   CH10_ENTFA              Reviewed;          94 AA.
AC   Q93EU7;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Co-chaperonin GroES {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Chaperonin-10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE            Short=Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Name=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groS {ECO:0000255|HAMAP-Rule:MF_00580}; OrderedLocusNames=EF_2634;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29212 / DSM 2570;
RX   PubMed=11526171; DOI=10.1128/jcm.39.9.3326-3331.2001;
RA   Teng L.-J., Hsueh P.R., Wang Y.H., Lin H.M., Luh K.T., Ho S.W.;
RT   "Determination of Enterococcus faecalis groESL full-length sequence and
RT   application for species identification.";
RL   J. Clin. Microbiol. 39:3326-3331(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Together with the chaperonin GroEL, plays an essential role
CC       in assisting protein folding. The GroEL-GroES system forms a nano-cage
CC       that allows encapsulation of the non-native substrate proteins and
CC       provides a physical environment optimized to promote and accelerate
CC       protein folding. GroES binds to the apical surface of the GroEL ring,
CC       thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-
CC       Rule:MF_00580}.
CC   -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. Interacts with the
CC       chaperonin GroEL. {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580}.
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DR   EMBL; AF335185; AAL04032.1; -; Genomic_DNA.
DR   EMBL; AE016830; AAO82343.1; -; Genomic_DNA.
DR   RefSeq; NP_816273.1; NC_004668.1.
DR   RefSeq; WP_002356531.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q93EU7; -.
DR   SMR; Q93EU7; -.
DR   STRING; 226185.EF_2634; -.
DR   EnsemblBacteria; AAO82343; AAO82343; EF_2634.
DR   GeneID; 60894631; -.
DR   KEGG; efa:EF2634; -.
DR   PATRIC; fig|226185.45.peg.925; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_2_1_9; -.
DR   OMA; EVKYSGE; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd00320; cpn10; 1.
DR   Gene3D; 2.30.33.40; -; 1.
DR   HAMAP; MF_00580; CH10; 1.
DR   InterPro; IPR020818; Chaperonin_GroES.
DR   InterPro; IPR037124; Chaperonin_GroES_sf.
DR   InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   PANTHER; PTHR10772; PTHR10772; 1.
DR   Pfam; PF00166; Cpn10; 1.
DR   PRINTS; PR00297; CHAPERONIN10.
DR   SMART; SM00883; Cpn10; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..94
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174753"
FT   CONFLICT        31
FT                   /note="K -> Q (in Ref. 1; AAL04032)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   94 AA;  10165 MW;  935D184E547E3DCC CRC64;
     MLKPLGDRVV IRVAKEEEKT VGGIVLASVA KEKPQTGEVI AVGEGRVLEN GTKVPMEVKI
     GDTVMFEKYS GTEVKYEGVE YLIVSAKDII ATVE